We report the kinetics and molecular properties of CD38 purified from bovine lung microsomal membranes after its solubilization with Triton X-100. The enzyme was found to be a novel member of a multicatalytic NAD+ - glycohydrolase (NADase, EC 3.2.2.6). It was able to utilize NAD+ in different ways, producing nicotinamide (Nam) and either adenosine diphosphoribose (ADPR, NADase activity) or cyclic ADPR (cADPR, cyclase activity); it also catalyzed the hydrolysis of cADPR to ADPR (cADPR, hydrolase activity). In addition, the enzyme catalyzed the pyridine base exchange reaction with conversion of NAD+ into NAD analogues. These data are evidence that CD38 is involved in the regulation of both NAD+ and calcium mobilizing agents, the concentration resulting in an essential enzyme that plays a key role in cellular energy and signal-transduction systems.
CD38 in bovine lung: a multicatalytic NADase
POLZONETTI, Valeria;PUCCIARELLI, Stefania;VITA, Alberto;VINCENZETTI, Silvia;NATALINI, Paolo
2009-01-01
Abstract
We report the kinetics and molecular properties of CD38 purified from bovine lung microsomal membranes after its solubilization with Triton X-100. The enzyme was found to be a novel member of a multicatalytic NAD+ - glycohydrolase (NADase, EC 3.2.2.6). It was able to utilize NAD+ in different ways, producing nicotinamide (Nam) and either adenosine diphosphoribose (ADPR, NADase activity) or cyclic ADPR (cADPR, cyclase activity); it also catalyzed the hydrolysis of cADPR to ADPR (cADPR, hydrolase activity). In addition, the enzyme catalyzed the pyridine base exchange reaction with conversion of NAD+ into NAD analogues. These data are evidence that CD38 is involved in the regulation of both NAD+ and calcium mobilizing agents, the concentration resulting in an essential enzyme that plays a key role in cellular energy and signal-transduction systems.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
